An aqueous H+ permeation pathway in the voltage-gated proton channel Hv1
نویسندگان
چکیده
منابع مشابه
Selectivity Mechanism of the Voltage-gated Proton Channel, HV1
Voltage-gated proton channels, HV1, trigger bioluminescence in dinoflagellates, enable calcification in coccolithophores, and play multifarious roles in human health. Because the proton concentration is minuscule, exquisite selectivity for protons over other ions is critical to HV1 function. The selectivity of the open HV1 channel requires an aspartate near an arginine in the selectivity filter...
متن کاملThe Voltage-Gated Proton Channel Hv1 Has Two Pores, Each Controlled by One Voltage Sensor
In voltage-gated channels, ions flow through a single pore located at the interface between membrane-spanning pore domains from each of four subunits, and the gates of the pore are controlled by four peripheral voltage-sensing domains. In a striking exception, the newly discovered voltage-gated Hv1 proton channels lack a homologous pore domain, leaving the location of the pore unknown. Also unk...
متن کاملVoltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains
Voltage-gated sodium, potassium, and calcium channels are made of a pore domain (PD) controlled by four voltage-sensing domains (VSDs). The PD contains the ion permeation pathway and the activation gate located on the intracellular side of the membrane. A large number of small molecules are known to inhibit the PD by acting as open channel blockers. The voltage-gated proton channel Hv1 is made ...
متن کاملThe Voltage-gated Proton Channel Hv1 Is Required for Insulin Secretion in Pancreatic β Cells
متن کامل
Temperature dependence of proton permeation through a voltage-gated proton channel
Voltage-gated proton channels are found in many different types of cells, where they facilitate proton movement through the membrane. The mechanism of proton permeation through the channel is an issue of long-term interest, but it remains an open question. To address this issue, we examined the temperature dependence of proton permeation. Under whole cell recordings, rapid temperature changes w...
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ژورنال
عنوان ژورنال: Nature Structural & Molecular Biology
سال: 2010
ISSN: 1545-9993,1545-9985
DOI: 10.1038/nsmb.1826